Identification of critical amino acid residues for chloride binding of Bacillus licheniformis trehalose-6-phosphate hydrolase

@article{Ong2013IdentificationOC,
  title={Identification of critical amino acid residues for chloride binding of Bacillus licheniformis trehalose-6-phosphate hydrolase},
  author={Ping-Lin Ong and Tzu-Ting Chuang and T H Wang and Long-Liu Lin},
  journal={Biologia},
  year={2013},
  volume={69},
  pages={1-9}
}
Based on sequence alignment of selected Cl− dependent and independent glycoside hydrolase family 13 enzymes, two invariant residues (Arg201 and Asn347) and one tyrosine (Tyr365) that might be responsible for the binding of Bacillus licheniformis trehalose-6-phosphate hydrolase (BlTreA) to chloride ion were identified. The role of these three residues was further explored by mutational and biophysical analyses. The mutant enzymes (R201Q/E/K, N327Q/D/K, and Y365A/R) and BlTreA were individually… CONTINUE READING